Suppr超能文献

阿莫西林酶法合成中酶固定化及堵塞机制的研究。

Investigation of Enzyme Immobilization and Clogging Mechanisms in the Enzymatic Synthesis of Amoxicillin.

机构信息

College of Food and Biology, Hebei University of Science and Technology, Shijiazhuang 050018, China.

出版信息

Int J Mol Sci. 2024 Aug 6;25(16):8557. doi: 10.3390/ijms25168557.

Abstract

This study investigated the blocking mechanism of immobilized penicillin G acylase (PGA) during the enzymatic synthesis of amoxicillin. Laboratory observations revealed that the primary cause of clogging was the crystallization of the substrate and product on the enzyme surface. Adjusting key parameters can significantly reduce clogging and improve catalytic efficiency. Methanol can decrease enzyme activity, but isopropyl alcohol cleaners can effectively remove clogs and protect enzyme activity. These findings provide an experimental foundation for optimizing the PGA immobilization process, which is crucial for achieving high efficiency and sustainability in industrial production.

摘要

本研究考察了固定化青霉素 G 酰化酶(PGA)在阿莫西林酶促合成过程中的阻断机制。实验室观察表明,堵塞的主要原因是底物和产物在酶表面结晶。调整关键参数可以显著减少堵塞并提高催化效率。甲醇会降低酶活性,但异丙醇清洁剂可以有效地清除堵塞物并保护酶活性。这些发现为优化 PGA 固定化过程提供了实验基础,对于实现工业生产的高效率和可持续性至关重要。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ccee/11354056/6bc66709c170/ijms-25-08557-g001.jpg

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验